This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. The enzymes involved in converting UDP-GlcA to other UDP-sugars are well described in eukaryotes, but less is known in prokaryotes. Here we identify and characterize a gene (RsU4kpxs) from Ralstonia solanacearum str. GMI1000, which encodes a dual-function enzyme, UDP-4-keto-pentose/UDP-xylose synthase (UXS). One activity is to decarboxylate UDP-glucuronic acid to UDP-[unreadable]-L-threo-pentopyranosyl-4"-ulose (UDP-4-keto-pentose) in the presence of NAD+. The second converts UDP-4-keto-pentose and NADH to UDP-xylose and NAD+, albeit at a lower rate. The identification of the R. solanacearum enzyme enables us to propose that the ancestral UXS (as well as UDP-apiose synthase or UAXS) diverged into two distinct enzymatic activities in early bacteria. This separation gave rise to the current Uxs in animal, fungus and plant as well as to the plant Uaxs homologs.